Nuclear magnetic resonance 15N and 1H resonance assignments and global fold of rusticyanin. Insights into the ligation and acid stability of the blue copper site.

Abstract

Nuclear magnetic resonance assignments are reported at pH approximately 3 for a type 1 ("blue") copper protein, rusticyanin, obtained from the acidophilic organism Thiobacillus ferrooxidans. A combination of homonuclear proton and heteronuclear 15N-edited NMR spectra has been used to assign most of the 1H and 15N resonances of reduced rusticyanin. The… (More)

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@article{Hunt1994NuclearMR, title={Nuclear magnetic resonance 15N and 1H resonance assignments and global fold of rusticyanin. Insights into the ligation and acid stability of the blue copper site.}, author={Adam Hunt and A Toy-Palmer and Nuria Assa-Munt and James Cavanagh and Richard Cameron Blake and H Jane Dyson}, journal={Journal of molecular biology}, year={1994}, volume={244 4}, pages={370-84} }